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SUMO‐binding sites in Nrf2
Author(s) -
Walters Treniqka,
Arinze Ifeanyi J
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.782.5
Subject(s) - sumo protein , transactivation , transcription factor , acetylation , promoter , binding site , sumo enzymes , chemistry , keap1 , phosphorylation , mutagenesis , posttranslational modification , microbiology and biotechnology , biology , biochemistry , gene , gene expression , mutation , ubiquitin , enzyme
The transcription factor Nrf2 influences transcription by binding to the antioxidant response element(s) (AREs) in target gene promoters, enabling oxidatively stressed cells to mount a response to oxidative stress in order to restore redox homeostasis. Post‐translational modifications (PTMs) that mediate release of Nrf2 from its inhibitory protein Keap1 have been extensively studied but PTMs that impact its biology after this release are just beginning to emerge. In this regard, only phosphorylation and acetylation have been previously reported. We recently found that Nrf2 can also be sumoylated. Here, we used three SUMO site‐predicting algorithms (SeeSUMO, SUMOsp and SUMOplot) to identify putative SUMO‐binding sites in Nrf2. Of the eight high probability sites identified by these algorithms, we found, using site‐directed mutagenesis and Co‐IP assay, that K 525 is a SUMO‐targeted site. This site binds SUMO‐2/3. The impact of sumoylation on the transactivation potential and degradation of Nrf2 are shown here. Supported by NIH grants SC1CA143985 and 5T32 GM07628–34.